Evidence map›Paper›PMID 16326909›Full record

ArticleBiophysical journal2006

Lifetime measurements reveal kinetic differences between homophilic cadherin bonds.

Marco V Bayas, Andrew Leung, Evan Evans, Deborah Leckband

Abstract read
In one paragraph

Article in Biophysical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

33 citing papers in PubMed.

  1. Article
  2. Engineering the Interactions of Classical Cadherin Cell-Cell Adhesion Proteins.Journal of immunology (Baltimore, Md. : 1950) · 2023
    Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Tuning the kinetics of cadherin adhesion.The Journal of investigative dermatology · 2013
    Review
  12. Article
  13. Cadherin recognition and adhesion.Current opinion in cell biology · 2012
    Review
  14. Article
  15. Review
  16. Regulation of catch bonds by rate of force application.The Journal of biological chemistry · 2011
    Article
  17. Multiphoton flow cytometry to assess intrinsic and extrinsic fluorescence in cellular aggregates: applications to stem cells.Microscopy and microanalysis : the official journal of Microscopy Society of America, Microbeam Analysis Society, Microscopical Society of Canada · 2011
    Article
  18. Review
  19. Article
  20. Biomembrane force probe investigation of RNA dissociation.European biophysics journal : EBJ · 2011
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors.

Marco V BayasCenter for Biophysics and Computational Biology, University of Illinois at Urbana-Champaign, Urbana, Illinois, USA.
Andrew Leung
Evan Evans
Deborah Leckband

Funding

RHEOLOGICAL AND ADHERENCE PROPERTIES OF SICKLE CELLSR01HL031579 · NHLBI · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI NARLA, MOHANDAS · 1985 to 2010
$3.8M
DYNAMIC STRENGTHS OF SINGLE LEUKOCYTE ADHESION BONDSR01HL065333 · NHLBI · BOSTON UNIVERSITY (CHARLES RIVER CAMPUS) · PI EVANS, EVAN A · 2001 to 2011
$3.0M
The Molecular Basis of Cadherin AdhesionR01GM051338 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI LECKBAND, DEBORAH E · 1999 to 2006
$1.6M
NHLBI NIH HHS HL31579NHLBI NIH HHS HL65333NHLBI NIH HHS R01 HL031579NHLBI NIH HHS R01 HL065333NIGMS NIH HHS 5 R01 GM51338NIGMS NIH HHS R01 GM051338
6 · The paper itself

Abstract

Cadherins are multidomain adhesion proteins whose interactions direct cell sorting during histogenesis. They determine cell adhesion specificity, but prior studies failed to identify physical differences that could underlie cell sorting. These single molecule studies identify kinetic and strength differences between different cadherins. They further demonstrate that the modular extracellular architecture of cleavage stage C-cadherin supports a multistate binding mechanism. These multiple bonds exhibit a kinetic hierarchy of strengths that map to the different cadherin domains. The outer two N-terminal domains of C-cadherin form two bound states with dissociation rates of 3.9 and 0.02 s(-1). The latter is 25-fold slower than between the corresponding epithelial cadherin segments. In addition to the two fast bonds, the five-domain fragment (CEC1-5) forms two additional stronger, longer-lived bonds with dissociation rates of 0.00039 and 0.00001 s(-1). We further quantified the lifetimes of bonds subject to a constant force, and thus identified multiple dissociation events with rates that agree quantitatively with the force spectroscopy data. The qualitative features are similar to those reported for epithelial cadherin. However, the significant differences in the dissociation rates of the outer domains, which include the specificity-determining region, suggest that kinetic differences may determine cadherin discrimination, rather than adhesion energies.

Indexed as

Models, BiologicalAnimalsBiomechanical PhenomenaCadherinsCHO CellsCricetinaeCricetulusErythrocytesKineticsProtein BindingProtein Structure, TertiaryRecombinant ProteinsXenopus laevisXenopus ProteinsCadherinsRecombinant ProteinsXenopus Proteins

Identifiers

PMID16326909
PMCPMC1367289

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.